2a5y | pdb_00002a5y
Structure of a CED-4/CED-9 complex
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| 2a5y, resolution 2.6Å | |||||||||||||
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| Ligands: | MG and ATP | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
Interplay among four genes--egl-1, ced-9, ced-4 and ced-3--controls the onset of programmed cell death in the nematode Caenorhabditis elegans. Activation of the cell-killing protease CED-3 requires CED-4. However, CED-4 is constitutively inhibited by CED-9 until its release by EGL-1. Here we report the crystal structure of the CED-4-CED-9 complex at 2.6 A resolution, and a complete reconstitution of the CED-3 activation pathway using homogeneous proteins of CED-4, CED-9 and EGL-1. One molecule of CED-9 binds to an asymmetric dimer of CED-4, but specifically recognizes only one of the two CED-4 molecules. This specific interaction prevents CED-4 from activating CED-3. EGL-1 binding induces pronounced conformational changes in CED-9 that result in the dissociation of the CED-4 dimer from CED-9. The released CED-4 dimer further dimerizes to form a tetramer, which facilitates the autoactivation of CED-3. Together, our studies provide important insights into the regulation of cell death activation in C. elegans.
About this Structure
2A5Y is a Protein complex structure of sequences from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans., Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y, Nature. 2005 Oct 6;437(7060):831-7. PMID:16208361
Page seeded by OCA on Sun Mar 23 14:34:55 2008
